Area:
Biochemistry, Pharmacology, Neuroscience Biology
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High-probability grants
According to our matching algorithm, John E. Maggio is the likely recipient of the following grants.
Years |
Recipients |
Code |
Title / Keywords |
Matching score |
1986 — 1993 |
Maggio, John E |
R01Activity Code Description: To support a discrete, specified, circumscribed project to be performed by the named investigator(s) in an area representing his or her specific interest and competencies. |
Tachykinins and Tachykinin Receptors @ Harvard University (Medical School)
The bioactive peptide substance P is an important mediator of a wide variety of functions in a wide variety of systems. Althoug substance P belongs to a family of peptides (the tachykinins), it was believed until recently to be the only member of that family in mammals. Implicit in most of the research on substance P was the assumption that no other tachykinins exist in mammals. In 1983, we reported that mammalian tissues contain not only substance P, but also substance K and neuromedin K. We have gone on to show that the three tachykinins have different tissue distributions and different receptors. The discovery of the new tachykinins has cast much of previous substance P research in some doubt, because the great structural similarity of these three peptides probably means that many of the biological functions now thought to be mediated by substance P may in fact be mediated by one of the new peptides. The tools used in substance P research up to now (e.g. the antagonists used in pharmacological studies and the antisera used in immunohistochemical studies) lack the specificity to descriminate between the three mammalian tachykinins. The goal is to further develop and apply techniques for tachykinin research that do have the specificity to discriminate between the various members of the peptide family. Using novel specific antisera for immunocytochemistry (specific aim 1) and novel specific radioligands for receptor studies (specific aim 2), we will be able to confirm (or correct) some current theories about substance P and extent tachykinin research to include all members of the peptide family. Only by the application of such techniques can the vast efforts already invested in substance P research over the last half-century be fully exploited. The significance of the proposed studies is the development of those specific tools and techniques, which will be crucial to research in a wide variety of systems (inflammation, nociception, smooth muscle, etc.) in which tachykinins play an important role.
|
0.939 |
1995 — 2005 |
Maggio, John E |
R01Activity Code Description: To support a discrete, specified, circumscribed project to be performed by the named investigator(s) in an area representing his or her specific interest and competencies. |
Amyloid Peptide Conformation and Amyloidosis @ University of Cincinnati
DESCRIPTION (From the Applicant's Abstract): The family of human diseases termed amyloidoses have the common feature that naturally occurring, normally innocuous soluble peptides or proteins assemble into particularly stable insoluble polymers which accumulate, increase in mass, and cause damage to surrounding tissue. Growth of the amyloid deposits is the hallmark pathological process of these diseases, but its mechanism is poorly understood. A major hurdle frustrating attempts to understand this process has been the lack of a simply and highly reproducible model system, which allows study of the deposition and dissociation kinetics at short timescale under a variety of conditions. Such a system would allow the essential thermodynamics of the processes to be worked out, and reaction steps vulnerable to therapeutic intervention identified. We have now developed such a system for studying the detailed kinetics of amyloid growth in a tissue-free system suitable for high throughput work. We have chosen to focus on the Ab amyloid of Alzheimer's disease, which makes up the brain senile plaques in this ailment, but a detailed knowledge of the deposition process will have implication for other diseases of protein misfolding. The determination of rate constants and activation entropies, enthalpies, and free energies of the template-mediated conformational changes from soluble to solid phase associated with amyloid growth, and the role of perturbations in structure and environment on these parameters, will be the major goal of these studies. Experimental determination of the kinetic parameters of a pathological folding transition involved in a human disease under physiological concentrations and conditions has not previously been possible. As a secondary aim, we will also examine the geometry of the peptide monomer within the amyloid fibril by photocrosslinking. Conclusions from the in vitro studies will be tested in human Alzheimer's disease brain sections.
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1 |